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Literature summary for 2.7.7.27 extracted from

  • Boehlein, S.K.; Shaw, J.R.; Stewart, J.D.; Hannah, L.C.
    Characterization of an autonomously activated plant adenosine diphosphate glucose pyrophosphorylase (2008), Plant Physiol., 149, 318-326.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.27

Activating Compound

Activating Compound Comment Organism Structure
3-phosphoglycerate activation of mutant Mos(1-198) is reduced compared to the wild-type enzyme, overview Zea mays
ADP-D-glucose activation of mutant Mos(1-198) is reduced compared to the wild-type enzyme, overview Solanum tuberosum
additional information mutant Mos(1-198) naturally occurs in a semiactivated state in the absence of an activator Zea mays
additional information mutant Mos(1-198) naturally occurs in a semiactivated state in the absence of an activator Solanum tuberosum

Protein Variants

Protein Variants Comment Organism
F332S site-directed mutagenesis in the potato part of the chimeric mutant Zea mays
F332S site-directed mutagenesis in the potato part of the chimeric mutant Solanum tuberosum
H341Y site-directed mutagenesis in the potato part of the chimeric mutant Zea mays
H341Y site-directed mutagenesis in the potato part of the chimeric mutant Solanum tuberosum
I323V site-directed mutagenesis in the potato part of the chimeric mutant Zea mays
I323V site-directed mutagenesis in the potato part of the chimeric mutant Solanum tuberosum
additional information expression of the maize/potato small subunit mosaic mutant MP, Mos(1-198), containing the first 198 amino acids of the small subunit of the maize endosperm enzyme and the last 277 amino acids from the potato tuber enzyme, Mos(1-198) and its derivatives are expressed exclusively with the wild-type maize large subunit, SH2. In the absence of activator, performs like a wild-type AGPase that is partially activated with 3-phosphoglycerate, enzymatic activity in the absence of 3-phosphoglycerate is substantially 2-5fold higher than that of wild-type enzyme, while in presence of 3-phosphoglycerate, Mos(1-198) AGPase activity is actually less than that of wild-type enzyme, phenotype, mutant Mos(1-198) naturally occurs in a semiactivated state in the absence of an activator, overview. Mutational exchange of carboxylterminal region containing 15 polymorphic amino acids from 377 to 475 to create Mos(1-198, 430-475) and Mos(1-198, 377-429) leading to reduced enzyme activity independent of 3-phosphoglycerate. Constructed mutant Mos(1-277) exhibits 3-phosphoglycerate-independent activity that is less than mutant Mos(1-198) and wild-type activity. Mutant Mos(1-321) has no detectible activity in the absence of 3-phosphoglycerate. In the presence of 3-phosphoglycerate however, Mos(1-321) activity in the reverse direction is identical to that of Mos(1-277), overview Zea mays
additional information expression of the maize/potato small subunit mosaic mutant MP, Mos(1-198), containing the first 198 amino acids of the small subunit of the maize endosperm enzyme and the last 277 amino acids from the potato tuber enzyme, Mos(1-198) and its derivatives are expressed exclusively with the wt maize large subunit, SH2. In the absence of activator, performs like a wild-type AGPase that is partially activated with ADP-D-glucose, enzymatic activity in the absence of 3-phosphoglycerate is substantially 2-5fold higher than that of wild-type enzyme, while in presence of 3-phosphoglycerate, Mos(1-198) AGPase activity is actually less than that of wild-type enzyme, phenotype, mutant Mos(1-198) naturally occurs in a semiactivated state in the absence of an activator, overview. Mutational exchange of carboxylterminal region containing 15 polymorphic amino acids from 377 to 475 to create Mos(1-198, 430-475) and Mos(1-198, 377-429) leading to reduced enzyme activity independent of 3-phosphoglycerate. Constructed mutant Mos(1-277) exhibits 3-phosphoglycerate-independent activity that is less than mutant Mos(1-198) and wild-type activity. Mutant Mos(1-321) has no detectible activity in the absence of 3-phosphoglycerate. In the presence of 3-phosphoglycerate however, Mos(1-321) activity in the reverse direction is identical to that of Mos(1-277), overview Solanum tuberosum
N369H site-directed mutagenesis in the potato part of the chimeric mutant Zea mays
N369H site-directed mutagenesis in the potato part of the chimeric mutant Solanum tuberosum
V347M site-directed mutagenesis in the potato part of the chimeric mutant Zea mays
V347M site-directed mutagenesis in the potato part of the chimeric mutant Solanum tuberosum

General Stability

General Stability Organism
bovine serum albumin stabilizes the purified enzyme at 0.5 mg/ml Zea mays
bovine serum albumin stabilizes the purified enzyme at 0.5 mg/ml Solanum tuberosum

Inhibitors

Inhibitors Comment Organism Structure
phosphate mutant Mos(1-198) is significantly inhibited in the absence of 3-phosphoglycerate even at low phosphate concentrations. Inhibition levels of wild-type and deletion mutants by phosphate, overview Solanum tuberosum
phosphate mutant Mos(1-198) is significantly inhibited in the absence of 3-phosphoglycerate even at low Pi concentrations. Inhibition levels of wild-type and deletion mutants by phosphate, overview Zea mays

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.018
-
 ATP pH 7.4, 37°C, mutant Mos(1-198), in absence of 3-phosphoglycerate Zea mays
0.018
-
 ATP pH 7.4, 37°C, mutant Mos(1-198), in absence of 3-phosphoglycerate Solanum tuberosum
0.039
-
 ATP pH 7.4, 37°C, mutant Mos(1-198, 430-475), in absence of 3-phosphoglycerate Zea mays
0.039
-
 ATP pH 7.4, 37°C, mutant Mos(1-198, 430-475), in absence of 3-phosphoglycerate Solanum tuberosum
0.04
-
 ATP pH 7.4, 37°C, mutant Mos(1-198, 377-429), in absence of 3-phosphoglycerate Zea mays
0.04
-
 ATP pH 7.4, 37°C, mutant Mos(1-198, 377-429), in absence of 3-phosphoglycerate Solanum tuberosum
0.04
-
 ATP pH 7.4, 37°C, mutant Mos(1-376), in absence of 3-phosphoglycerate Zea mays
0.04
-
 ATP pH 7.4, 37°C, mutant Mos(1-376), in absence of 3-phosphoglycerate Solanum tuberosum
0.044
-
 ATP pH 7.4, 37°C, mutant Mos(1-277), in absence of 3-phosphoglycerate Zea mays
0.044
-
 ATP pH 7.4, 37°C, mutant Mos(1-277), in absence of 3-phosphoglycerate Solanum tuberosum
0.051
-
 ATP pH 7.4, 37°C, mutant Mos(1-198), in presence of 3-phosphoglycerate Zea mays
0.051
-
 ATP pH 7.4, 37°C, mutant Mos(1-198), in presence of 3-phosphoglycerate Solanum tuberosum
0.056
-
 ATP pH 7.4, 37°C, mutant Mos(1-198, 377-475), in absence of 3-phosphoglycerate Zea mays
0.056
-
 ATP pH 7.4, 37°C, mutant Mos(1-198, 377-475), in absence of 3-phosphoglycerate Solanum tuberosum
0.074
-
 ATP pH 7.4, 37°C, wild-type enzyme, in presence of 3-phosphoglycerate Zea mays
0.074
-
 ATP pH 7.4, 37°C, wild-type enzyme, in presence of 3-phosphoglycerate Solanum tuberosum
0.075
-
 ATP pH 7.4, 37°C, wild-type enzyme, in absence of 3-phosphoglycerate Zea mays
0.075
-
 ATP pH 7.4, 37°C, wild-type enzyme, in absence of 3-phosphoglycerate Solanum tuberosum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Zea mays
Mg2+
-
 Solanum tuberosum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + alpha-D-glucose 1-phosphate Zea mays
-
 ADP-D-glucose + diphosphate
-
 r
ATP + alpha-D-glucose 1-phosphate Solanum tuberosum
-
 ADP-D-glucose + diphosphate
-
 r

Organism

Organism UniProt Comment Textmining
Solanum tuberosum
-
-
-
Zea mays
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant AGPases using protamine sulfate and ammonium sulfate fractionation, followed by ion exchange and hydroxyapatite chromatography Zea mays
recombinant wild-type and mutant AGPases using protamine sulfate and ammonium sulfate fractionation, followed by ion exchange and hydroxyapatite chromatography Solanum tuberosum

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Zea mays
-
leaf
-
 Solanum tuberosum
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.72
-
 purified mutant Mos(1-198, 377-475) in absence of 3-phosphoglycerate Zea mays
0.72
-
 purified mutant Mos(1-198, 377-475) in absence of 3-phosphoglycerate Solanum tuberosum
1.47
-
 purified mutant Mos(1-376) in absence of 3-phosphoglycerate Zea mays
1.47
-
 purified mutant Mos(1-376) in absence of 3-phosphoglycerate Solanum tuberosum
1.68
-
 purified mutant Mos(1-198, 430-475) in absence of 3-phosphoglycerate Zea mays
1.68
-
 purified mutant Mos(1-198, 430-475) in absence of 3-phosphoglycerate Solanum tuberosum
1.78
-
 purified mutant Mos(1-198, 377-429) in absence of 3-phosphoglycerate Zea mays
1.78
-
 purified mutant Mos(1-198, 377-429) in absence of 3-phosphoglycerate Solanum tuberosum
1.8
-
 purified mutant Mos(1-277) in absence of 3-phosphoglycerate Zea mays
1.8
-
 purified mutant Mos(1-277) in absence of 3-phosphoglycerate Solanum tuberosum
2.45
-
 purified wild-type enzyme, in absence of 3-phosphoglycerate Zea mays
2.45
-
 purified wild-type enzyme, in absence of 3-phosphoglycerate Solanum tuberosum
4.87
-
 purified mutant Mos(1-198) in absence of 3-phosphoglycerate Zea mays
4.87
-
 purified mutant Mos(1-198) in absence of 3-phosphoglycerate Solanum tuberosum
6.14
-
 purified mutant Mos(1-198, 430-475) in presence of 3-phosphoglycerate Zea mays
6.14
-
 purified mutant Mos(1-198, 430-475) in presence of 3-phosphoglycerate Solanum tuberosum
6.81
-
 purified mutant Mos(1-198, 377-429) in presence of 3-phosphoglycerate Zea mays
6.81
-
 purified mutant Mos(1-198, 377-429) in presence of 3-phosphoglycerate Solanum tuberosum
7.29
-
 purified mutant Mos(1-277) in presence of 3-phosphoglycerate Zea mays
7.29
-
 purified mutant Mos(1-277) in presence of 3-phosphoglycerate Solanum tuberosum
8.59
-
 purified mutant Mos(1-198, 377-475) in presence of 3-phosphoglycerate Zea mays
8.59
-
 purified mutant Mos(1-198, 377-475) in presence of 3-phosphoglycerate Solanum tuberosum
9.38
-
 purified mutant Mos(1-376) in presence of 3-phosphoglycerate Zea mays
9.38
-
 purified mutant Mos(1-376) in presence of 3-phosphoglycerate Solanum tuberosum
10.87
-
 purified mutant Mos(1-198) in presence of 3-phosphoglycerate Zea mays
10.87
-
 purified mutant Mos(1-198) in presence of 3-phosphoglycerate Solanum tuberosum
21.81
-
 purified wild-type enzyme in presence of 3-phosphoglycerate Zea mays
21.81
-
 purified wild-type enzyme in presence of 3-phosphoglycerate Solanum tuberosum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + alpha-D-glucose 1-phosphate
-
 Zea mays ADP-D-glucose + diphosphate
-
 r
ATP + alpha-D-glucose 1-phosphate
-
 Solanum tuberosum ADP-D-glucose + diphosphate
-
 r
ATP + alpha-D-glucose 1-phosphate substrate binding structure and kinetics, regulation of wild-type and mutant enzymes, mapping the polymorphic sites important in altered allosteric properties, overview Zea mays ADP-D-glucose + diphosphate
-
 r
ATP + alpha-D-glucose 1-phosphate substrate binding structure and kinetics, regulation of wild-type and mutant enzymes, mapping the polymorphic sites important in altered allosteric properties, overview Solanum tuberosum ADP-D-glucose + diphosphate
-
 r

Synonyms

Synonyms Comment Organism
adenosine diphosphate glucose pyrophosphorylase
-
 Zea mays
adenosine diphosphate glucose pyrophosphorylase
-
 Solanum tuberosum
ADP-glucose pyrophosphorylase
-
 Zea mays
ADP-glucose pyrophosphorylase
-
 Solanum tuberosum
AGPase
-
 Zea mays
AGPase
-
 Solanum tuberosum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Zea mays
37
-
 assay at Solanum tuberosum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
42
-
 wild-type AGPAse in the absence of 3-phosphoglycerate has a half-life of 1 min, whereas mutant Mos(1-198) has a half-life of 5.5 min, when 3-phosphoglycerate is added to the wid-type enzyme, the half-life increases to 5.5 min and the half-life of the mutant is incrwased to 9.4 min Zea mays
42
-
 wild-type AGPAse in the absence of 3-phosphoglycerate has a half-life of 1 min, whereas mutant Mos(1-198) has a half-life of 5.5 min, when 3-phosphoglycerate is added to the wid-type enzyme, the half-life increases to 5.5 min and the half-life of the mutant is incrwased to 9.4 min Solanum tuberosum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Zea mays
7.4
-
 assay at Solanum tuberosum

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1
-
 phosphate the phosphate inhibition pattern of Mos(1-198) is complex and biphasic. Inhibition at relatively high phopshate concentrations is less than predicted at low phosphate concentrations, the calculated Ki for phosphate is about 1 mM before 50% inhibition and 36 mM after 50% inhibition. Inhibition kinetics of mutants in presence and absence of 3-phosphoglycerate Solanum tuberosum
1
-
 phosphate the phosphate inhibition pattern of Mos(1-198) is complex and biphasic. Inhibition at relatively high phosphate concentrations is less than predicted at low phosphate concentrations, the calculated Ki for phosphate is about1 mM before 50% inhibition and 36 mM after 50% inhibition. Inhibition kinetics of mutants in presence and absence of 3-phosphoglycerate Zea mays
1.4
-
 phosphate wild-type enzyme, in presence of 3-phosphoglycerate Zea mays
1.4
-
 phosphate wild-type enzyme, in presence of 3-phosphoglycerate Solanum tuberosum
8.7
-
 phosphate mutant Mos(1-198), in presence of 3-phosphoglycerate Zea mays
8.7
-
 phosphate mutant Mos(1-198), in presence of 3-phosphoglycerate Solanum tuberosum